Emma Sparr

This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.

The paper models the coupling between membrane bending and stretching in lipid vesicles, showing that thinning reduces bending energy and explains the lower limit of vesicle sizes.

This study uses PICUP to identify transient α-synuclein contacts in different conformational states, revealing state-specific interactions in solution, membrane-bound, and fibril forms.

This study investigates how lipid membranes influence the equilibrium between free and membrane-bound α-synuclein and its amyloid formation, revealing conditions that promote or inhibit aggregation.